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RNA-dependent ATPase from Saccharomyces cerevisiae [Yeasts]
A new RNA-dependent ATPase has been isolated from yeast chromatin extracts and partially characterized. The protein has a sedimentation coefficient of about 7 S. The enzyme hydrolyzes specifically ATP (or dATP) to ADP (or dADP) and Pi in the presence of Mg2+ or Mn2+ ions and requires a single-strand...
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| Published in: | The Journal of biological chemistry 1980-12, Vol.255 (24), p.11704-11709 |
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| Main Authors: | , , |
| Format: | Article |
| Language: | English |
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| container_end_page | 11709 |
| container_issue | 24 |
| container_start_page | 11704 |
| container_title | The Journal of biological chemistry |
| container_volume | 255 |
| creator | Belhadj, O Sentenac, A Fromageot, P |
| description | A new RNA-dependent ATPase has been isolated from yeast chromatin extracts and partially characterized. The protein has a
sedimentation coefficient of about 7 S. The enzyme hydrolyzes specifically ATP (or dATP) to ADP (or dADP) and Pi in the presence
of Mg2+ or Mn2+ ions and requires a single-stranded polynucleotide as cofactor. The order of efficiency of synthetic polymers
is poly(rU) > poly(rI) greater than or equal to poly(dU) > poly(rA) greater than or equal to poly(rC). Among natural polymers,
single-stranded DNA and poly(rA)-containing mRNA from yeast are also active but less so than poly(rU). The enzyme exhibits
a pH optimum of 8 and is fully inhibited by 0.25 M NaCl. The Km for ATP is0.2 mM. The resemblance between this ATPase and
DNA-dependent ATPases from other sources, as well as the termination factor rho, is discussed. |
| doi_str_mv | 10.1016/S0021-9258(19)70190-2 |
| format | article |
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sedimentation coefficient of about 7 S. The enzyme hydrolyzes specifically ATP (or dATP) to ADP (or dADP) and Pi in the presence
of Mg2+ or Mn2+ ions and requires a single-stranded polynucleotide as cofactor. The order of efficiency of synthetic polymers
is poly(rU) > poly(rI) greater than or equal to poly(dU) > poly(rA) greater than or equal to poly(rC). Among natural polymers,
single-stranded DNA and poly(rA)-containing mRNA from yeast are also active but less so than poly(rU). The enzyme exhibits
a pH optimum of 8 and is fully inhibited by 0.25 M NaCl. The Km for ATP is0.2 mM. The resemblance between this ATPase and
DNA-dependent ATPases from other sources, as well as the termination factor rho, is discussed.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/S0021-9258(19)70190-2</identifier><identifier>PMID: 6108325</identifier><language>eng</language><publisher>United States: American Society for Biochemistry and Molecular Biology</publisher><subject>Adenosine Triphosphatases - isolation & purification ; Adenosine Triphosphatases - metabolism ; Chromatin - enzymology ; DNA, Single-Stranded ; Kinetics ; Molecular Weight ; Polynucleotides - pharmacology ; Saccharomyces cerevisiae - enzymology ; Structure-Activity Relationship ; Substrate Specificity</subject><ispartof>The Journal of biological chemistry, 1980-12, Vol.255 (24), p.11704-11709</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c403t-f798588fa98cd4b1a740a7d82a29292c27baa2e9ec1a8fd3f7ba208338b285713</citedby><cites>FETCH-LOGICAL-c403t-f798588fa98cd4b1a740a7d82a29292c27baa2e9ec1a8fd3f7ba208338b285713</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/6108325$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Belhadj, O</creatorcontrib><creatorcontrib>Sentenac, A</creatorcontrib><creatorcontrib>Fromageot, P</creatorcontrib><creatorcontrib>Oklahoma State University(USA)</creatorcontrib><title>RNA-dependent ATPase from Saccharomyces cerevisiae [Yeasts]</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>A new RNA-dependent ATPase has been isolated from yeast chromatin extracts and partially characterized. The protein has a
sedimentation coefficient of about 7 S. The enzyme hydrolyzes specifically ATP (or dATP) to ADP (or dADP) and Pi in the presence
of Mg2+ or Mn2+ ions and requires a single-stranded polynucleotide as cofactor. The order of efficiency of synthetic polymers
is poly(rU) > poly(rI) greater than or equal to poly(dU) > poly(rA) greater than or equal to poly(rC). Among natural polymers,
single-stranded DNA and poly(rA)-containing mRNA from yeast are also active but less so than poly(rU). The enzyme exhibits
a pH optimum of 8 and is fully inhibited by 0.25 M NaCl. The Km for ATP is0.2 mM. The resemblance between this ATPase and
DNA-dependent ATPases from other sources, as well as the termination factor rho, is discussed.</description><subject>Adenosine Triphosphatases - isolation & purification</subject><subject>Adenosine Triphosphatases - metabolism</subject><subject>Chromatin - enzymology</subject><subject>DNA, Single-Stranded</subject><subject>Kinetics</subject><subject>Molecular Weight</subject><subject>Polynucleotides - pharmacology</subject><subject>Saccharomyces cerevisiae - enzymology</subject><subject>Structure-Activity Relationship</subject><subject>Substrate Specificity</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1980</creationdate><recordtype>article</recordtype><recordid>eNo9kFtLKzEQgIMc0Xr5CR724SD6sJpJNibBp1K8gahYBUUOYTY7a1e63Zq0iv_e1BaTh0yYb2aSj7E94EfA4eR4yLmA3AplDsAeag6W52KN9YAbmUsFT39Y7xfZZFsxvvG0CgsbbONkQQnVY6f3N_28oilNKprMsv7DHUbK6tC12RC9H2GKvjzFzFOgjyY2SNnLM2Gcxf87bL3GcaTd1bnNHs_PHgaX-fXtxdWgf537gstZXmtrlDE1WuOrogTUBUddGYHCpu2FLhEFWfKApq5kne4iPU-aUhilQW6z_WXfaeje5xRnrm2ip_EYJ9TNo9NKFunDJoFqCfrQxRiodtPQtBi-HHC3kOZ-pLmFEQfW_UhzItXtrQbMy5aq36qVpZT_t8yPmtfRZxPIlU3nR9Q6oZQThQPQvEjY3yVWY-fwNTTRPQ7BGsG1lCC4_AZm5Hsw</recordid><startdate>19801225</startdate><enddate>19801225</enddate><creator>Belhadj, O</creator><creator>Sentenac, A</creator><creator>Fromageot, P</creator><general>American Society for Biochemistry and Molecular Biology</general><scope>FBQ</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>19801225</creationdate><title>RNA-dependent ATPase from Saccharomyces cerevisiae [Yeasts]</title><author>Belhadj, O ; Sentenac, A ; Fromageot, P</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c403t-f798588fa98cd4b1a740a7d82a29292c27baa2e9ec1a8fd3f7ba208338b285713</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1980</creationdate><topic>Adenosine Triphosphatases - isolation & purification</topic><topic>Adenosine Triphosphatases - metabolism</topic><topic>Chromatin - enzymology</topic><topic>DNA, Single-Stranded</topic><topic>Kinetics</topic><topic>Molecular Weight</topic><topic>Polynucleotides - pharmacology</topic><topic>Saccharomyces cerevisiae - enzymology</topic><topic>Structure-Activity Relationship</topic><topic>Substrate Specificity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Belhadj, O</creatorcontrib><creatorcontrib>Sentenac, A</creatorcontrib><creatorcontrib>Fromageot, P</creatorcontrib><creatorcontrib>Oklahoma State University(USA)</creatorcontrib><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Belhadj, O</au><au>Sentenac, A</au><au>Fromageot, P</au><aucorp>Oklahoma State University(USA)</aucorp><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>RNA-dependent ATPase from Saccharomyces cerevisiae [Yeasts]</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1980-12-25</date><risdate>1980</risdate><volume>255</volume><issue>24</issue><spage>11704</spage><epage>11709</epage><pages>11704-11709</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>A new RNA-dependent ATPase has been isolated from yeast chromatin extracts and partially characterized. The protein has a
sedimentation coefficient of about 7 S. The enzyme hydrolyzes specifically ATP (or dATP) to ADP (or dADP) and Pi in the presence
of Mg2+ or Mn2+ ions and requires a single-stranded polynucleotide as cofactor. The order of efficiency of synthetic polymers
is poly(rU) > poly(rI) greater than or equal to poly(dU) > poly(rA) greater than or equal to poly(rC). Among natural polymers,
single-stranded DNA and poly(rA)-containing mRNA from yeast are also active but less so than poly(rU). The enzyme exhibits
a pH optimum of 8 and is fully inhibited by 0.25 M NaCl. The Km for ATP is0.2 mM. The resemblance between this ATPase and
DNA-dependent ATPases from other sources, as well as the termination factor rho, is discussed.</abstract><cop>United States</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>6108325</pmid><doi>10.1016/S0021-9258(19)70190-2</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| identifier | ISSN: 0021-9258 |
| ispartof | The Journal of biological chemistry, 1980-12, Vol.255 (24), p.11704-11709 |
| issn | 0021-9258 1083-351X |
| language | eng |
| recordid | cdi_proquest_miscellaneous_75343518 |
| source | ScienceDirect (Online service) |
| subjects | Adenosine Triphosphatases - isolation & purification Adenosine Triphosphatases - metabolism Chromatin - enzymology DNA, Single-Stranded Kinetics Molecular Weight Polynucleotides - pharmacology Saccharomyces cerevisiae - enzymology Structure-Activity Relationship Substrate Specificity |
| title | RNA-dependent ATPase from Saccharomyces cerevisiae [Yeasts] |
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